Martin J. Scanlon

TL;DR: It is shown that the MLKL pseudokinase domain acts as a latch to restrain the N-terminal four-helix bundle (4HB) domain and that unleashing this domain results in formation of a high-molecular-weight, membrane-localized complex and cell death.

TL;DR: A key step in the protein-folding pathway is the introduction of disulphide bonds between cysteine residues in a process called oxidative protein folding as discussed by the authors, which is a process that is essential for cell integrity and to produce virulence factors.

TL;DR: This view of protein-folding machinery must now be adjusted to encompass the wider range of disulphide catalytic systems present in bacteria.

TL;DR: Kalata B2 is the second putative member of the Mobius cyclotide family to be structurally characterized and has a cis-peptidyl-proline bond, thus validating the suggested name for this subfamily of cyclotides.

TL;DR: The three-dimensional structure of the human LDL receptor has been determined by two-dimensional NMR spectroscopy and shown to consist of a beta-hairpin structure, followed by a series of beta turns, which may represent a structural paradigm both for the other modules in the LDL receptor and for the homologous domains of several other proteins.